A G1 Glycoprotein Epitope of La Crosse Virus: a Determinant of Infection of Aedes triseriatus
| Autor: | Daniel R. Sundin, Neal Nathanson, Francisco Gonzalez-Scarano, Barry J. Beaty |
|---|---|
| Rok vydání: | 1987 |
| Předmět: |
La Crosse virus
Bunyaviridae viruses Encephalitis Virus California Biology Virus Replication Arbovirus Virus Microbiology Viral Envelope Proteins Viral envelope Aedes Neutralization Tests medicine Animals Vector (molecular biology) Antigens Viral Glycoproteins Multidisciplinary Host (biology) fungi Antibodies Monoclonal medicine.disease biology.organism_classification Virology Insect Vectors Intestines Viral replication |
| Zdroj: | Science. 235:591-593 |
| ISSN: | 1095-9203 0036-8075 |
| DOI: | 10.1126/science.3810159 |
| Popis: | Arthropod-borne viruses (arboviruses) have specific vector-vertebrate host cycles in nature. The molecular basis of restriction of virus replication to a very limited number of vector species is unknown, but the present study suggests that viral attachment proteins are important determinants of vector-virus interactions. The principal vector of La Crosse (LAC) virus is the mosquito Aedes triseriatus, and LAC virus efficiently infects the mosquito when ingested. However, a variant (V22) of LAC virus, which was selected by growing the virus in the presence of a monoclonal antibody, was markedly restricted in its ability to infect Ae. triseriatus when it was ingested. Only 15% of the mosquitoes that ingested V22 became infected and 5% of these developed disseminated infections. In contrast, 89% of the mosquitoes that ingested LAC became infected and 74% developed disseminated infections. When V22 was passed three times in mosquitoes by feeding, a revertant virus, V22M3, was obtained that infected 85% of Ae. triseriatus ingesting this virus. In addition, V22M3 regained the antigenic phenotype and fusion capability of the parent LAC virus. These results suggest that the specificity of LAC virus-vector interactions is markedly influenced by the efficiency of the fusion function of the G1 envelope glycoprotein operating at the midgut level in the arthropod vector. |
| Databáze: | OpenAIRE |
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